Structural comparison of the apo form of Saccharomyces cerevisiae anthranilate phosphoribosyltransferase with structures of its complexes with PRPP or the substrate analogue 4-fluoroanthranilate provide structural insights into substrate binding.

Orotate phosphoribosyltransferase from Plasmodium falciparum produced in Escherichia coli was crystallized by the sitting-drop vapour-diffusion method in complex with OA and PRPP in the presence of Mg²⁺.

The crystal structure of phosphoribosylpyrophosphate synthetase from a thermophilic strain of T. thermophilus was determined. An ADP molecule and a sulfate ion were located in the active site and a sulfate ion was located in the allosteric site.

P. falciparum orotate phosphoribosyltransferase, a potential target for antimalarial drugs and a conduit for prodrugs, crystallized as a structure with eight molecules per asymmetric unit that included some unique parasite-specific auto-inhibitory interactions between catalytic dimers.

Crystals of human PRPP synthetase 1 (PRS1) in complex with Mg²⁺, P_i and ATP were obtained and diffraction data were collected to 2.6 Å resolution.

Crystals of S. scrofa quinolinate phosphoribosyltransferase purified from porcine kidney in complex with nicotinate mononucleotidewere obtained and diffraction data were collected and processed to 2.1 Å resolution.

The structure of the methanofuran/methanopterin-biosynthetic enzyme (MJ1099) from M. jannaschii was determined at 1.7 Å resolution using anomalous scattering methods.

The crystal structure of OPRTase from the caries pathogen Streptococcus mutans is reported at 2.4 Å resolution.

The structure of uracil phosphoribosyltransferase from B. caldolyticus with bound UMP is described and a catalytic mechanism is proposed.

X-ray diffraction data have been collected from crystals of recombinant sugar cane phosphoribosylpyrophosphate synthase (PRS) and analysis has revealed its quaternary structure, localizing this PRS into the class of enzymes forming an hexameric oligomer of 223 kDa.